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6 results for “chaperone”

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  1. Neuronal aging causes mislocalization of splicing proteins and unchecked cellular stress.

    Nature neuroscience · 2025 · 28(6): 1174-1184

    Aging is one of the most prominent risk factors for neurodegeneration, yet the molecular mechanisms underlying the deterioration of old neurons are mostly unknown. To efficiently study neurodegeneration in the context of aging, we transdifferentiated primary human fibroblasts from aged …

    PMID 40456907 DOI ↗

  2. Localized molecular chaperone synthesis maintains neuronal dendrite proteostasis.

    Nature communications · 2024 · 15(1): 10796

    Proteostasis is maintained through regulated protein synthesis and degradation and chaperone-assisted protein folding. However, this is challenging in neuronal projections because of their polarized morphology and constant synaptic proteome remodeling. Using high-resolution fluorescence microscopy, we discover that hippocampal and spinal …

    PMID 39737952 DOI ↗

  3. Localized synthesis of molecular chaperones sustains neuronal proteostasis.

    bioRxiv : the preprint server for biology · 2024

    Neurons are challenged to maintain proteostasis in neuronal projections, particularly with the physiological stress at synapses to support intercellular communication underlying important functions such as memory and movement control. Proteostasis is maintained through regulated protein synthesis and degradation and chaperone-assisted …

    PMID 37873158 DOI ↗

  4. A phage nucleus-associated RNA-binding protein is required for jumbo phage infection.

    bioRxiv : the preprint server for biology · 2023

    Large-genome bacteriophages (jumbo phages) of the <i>Chimalliviridae</i> family assemble a nucleus-like compartment bounded by a protein shell that protects the replicating phage genome from host-encoded restriction enzymes and CRISPR/Cas nucleases. While the nuclear shell provides broad protection against host nucleases, …

    PMID 37790334 DOI ↗

  5. The <i>Thermus thermophilus</i> DEAD-box protein Hera is a general RNA binding protein and plays a key role in tRNA metabolism.

    RNA (New York, N.Y.) · 2020 · 26(11): 1557-1574

    RNA helicases catalyze the ATP-dependent destabilization of RNA duplexes. DEAD-box helicases share a helicase core that mediates ATP binding and hydrolysis, RNA binding and unwinding. Most members of this family contain domains flanking the core that can confer RNA substrate …

    PMID 32669294 DOI ↗

  6. Context-Dependent and Disease-Specific Diversity in Protein Interactions within Stress Granules.

    Cell · 2018 · 172(3): 590-604.e13

    Stress granules (SGs) are transient ribonucleoprotein (RNP) aggregates that form during cellular stress and are increasingly implicated in human neurodegeneration. To study the proteome and compositional diversity of SGs in different cell types and in the context of neurodegeneration-linked mutations, …

    PMID 29373831 DOI ↗

Datasets 5

GSE276986 GSE · GEO

Aging-linked deterioration of RNA metabolism destabilizes the stress response of neurons [RNA-seq]

Homo sapiens · GPL24676

GSE276985 GSE · GEO

Aging-linked deterioration of RNA metabolism destabilizes the stress response of neurons [eCLIP-seq]

Mus musculus · GPL24676

GSE277082 GSE · GEO

Aging-linked deterioration of RNA metabolism destabilizes the stress response of neurons [RNASeq, RiboSeq]

Homo sapiens · GPL24676

GSE135435 GSE · GEO

The Thermus thermophilus DEAD-box protein Hera is a general RNA chaperone and plays a key role in tRNA metabolism

Thermus thermophilus HB27 · GPL27012

GSE243675 GSE · GEO

A phage nucleus-associated RNA-binding protein required for jumbo phage infection

287 · GPL24583

Analyses 2

GSE202202 Processing Pipeline

GSE202202 · 4 steps · RNA-Seq · code_examples

Localized molecular chaperone synthesis maintains neuronal dendrite proteostasis. (2024)

GSE135435 Processing Pipeline

GSE135435 · 29 steps · RIP-Seq · code_examples

The <i>Thermus thermophilus</i> DEAD-box protein Hera is a general RNA binding protein and plays a key role in tRNA metabolism. (2020)